ID   RIHB_ECOLU              Reviewed;         313 AA.
AC   B7N5C5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Pyrimidine-specific ribonucleoside hydrolase RihB {ECO:0000255|HAMAP-Rule:MF_01433};
DE            EC=3.2.2.8 {ECO:0000255|HAMAP-Rule:MF_01433};
DE   AltName: Full=Cytidine/uridine-specific hydrolase {ECO:0000255|HAMAP-Rule:MF_01433};
GN   Name=rihB {ECO:0000255|HAMAP-Rule:MF_01433}; OrderedLocusNames=ECUMN_2498;
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or
CC       uracil, respectively. Has a clear preference for cytidine over uridine.
CC       Strictly specific for ribonucleosides. {ECO:0000255|HAMAP-
CC       Rule:MF_01433}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a pyrimidine ribonucleoside + H2O = a pyrimidine nucleobase +
CC         D-ribose; Xref=Rhea:RHEA:56816, ChEBI:CHEBI:15377, ChEBI:CHEBI:26432,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:141014; EC=3.2.2.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01433};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01433};
CC       Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01433};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01433}.
CC   -!- SIMILARITY: Belongs to the IUNH family. RihB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01433}.
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DR   EMBL; CU928163; CAR13684.1; -; Genomic_DNA.
DR   RefSeq; WP_000415440.1; NC_011751.1.
DR   RefSeq; YP_002413212.1; NC_011751.1.
DR   AlphaFoldDB; B7N5C5; -.
DR   SMR; B7N5C5; -.
DR   STRING; 585056.ECUMN_2498; -.
DR   EnsemblBacteria; CAR13684; CAR13684; ECUMN_2498.
DR   KEGG; eum:ECUMN_2498; -.
DR   PATRIC; fig|585056.7.peg.2678; -.
DR   HOGENOM; CLU_036838_2_0_6; -.
DR   OMA; REKAHEW; -.
DR   Proteomes; UP000007097; Chromosome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045437; F:uridine nucleosidase activity; IEA:UniProt.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046133; P:pyrimidine ribonucleoside catabolic process; IEA:InterPro.
DR   Gene3D; 3.90.245.10; -; 1.
DR   HAMAP; MF_01433; Pyrim_hydro_RihB; 1.
DR   InterPro; IPR015910; I/U_nuclsd_hydro_CS.
DR   InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR   InterPro; IPR023186; IUNH.
DR   InterPro; IPR022977; Pyrim_hydro_RihB.
DR   InterPro; IPR036452; Ribo_hydro-like.
DR   PANTHER; PTHR12304; PTHR12304; 1.
DR   Pfam; PF01156; IU_nuc_hydro; 1.
DR   SUPFAM; SSF53590; SSF53590; 1.
DR   PROSITE; PS01247; IUNH; 1.
PE   3: Inferred from homology;
KW   Calcium; Glycosidase; Hydrolase; Metal-binding.
FT   CHAIN           1..313
FT                   /note="Pyrimidine-specific ribonucleoside hydrolase RihB"
FT                   /id="PRO_1000145832"
FT   ACT_SITE        11
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT   BINDING         16
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT   BINDING         124
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
FT   BINDING         240
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01433"
SQ   SEQUENCE   313 AA;  33732 MW;  D6169889CB89E643 CRC64;
     MEKRKIILDC DPGHDDAIAI MMAAKHPVID LLGITIVAGN QTLDKTLING LNVCQKLEIN
     VPVYAGMPQP IMRQQIVADN IHGETGLDGP VFGPLTRQAE STHAVKYIID TLMASDGDIT
     LVPVGPLSNI AVAMRMQPAI LPKIREIVLM GGAYGTGNFT PSAEFNIFAD PEAARVVFTS
     GVPLVMMGLD LTNQTVCTPD VIARMERVGG PAGELFSDIM NFTLKTQFEN YGLAGGPVHD
     ATCIGYLINP DGIKTQEMYV EVDVNSGPCY GRTVCDELGV LGKPANTKVG ITIDTDWFWG
     LVEECVRGYI KTH